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Formation of native structure by intermolecular thiol‐disulfide exchange reactions without oxidants in the folding of bovine pancreatic ribonuclease A
Author(s) -
Song Myeong-Cheol,
Scheraga Harold A
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01386-7
Subject(s) - bovine pancreatic ribonuclease , oxidative folding , chemistry , disulfide bond , ribonuclease , disproportionation , intermolecular force , folding (dsp implementation) , protein folding , reagent , redox , thiol , protein disulfide isomerase , biochemistry , organic chemistry , molecule , catalysis , rna , electrical engineering , gene , engineering
It has been shown previously that the oxidative folding of bovine pancreatic ribonuclease A proceeds through parallel pathways with two major native‐like three‐disulfide (3S) intermediates. We show here that, under some conditions, the native disulfide bonds can also be regenerated through disproportionation reactions; in other words, the protein can serve as its own redox reagent. The results also show that disulfide species of the unstructured 3S ensemble have a strong propensity to participate in intermolecular interactions. These interactions are favored at high protein concentration, temperature and pH, and lead to formation of the native structure during disulfide reshuffling in the rate‐determining step.